EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.2.1.90 | D-glyceraldehyde 3-phosphate + NAD(P)+ + H2O |
the enzyme is part of the modified glycolytic pathway of Thermoproteus tenax. In the classical EmbdenÂMeyerhofÂParnas glycolysis, as found in Eucarya and Bacteria, the oxidation of D-glyceraldehyde 3-phosphate is coupled to phosphorylation to yield 1,3-diphosphoglycerate, which in turn is utilized by phosphoglycerate kinase giving 3-phosphoglycerate and ATP. These steps are reversible and non-regulated in the common EmbdenÂMeyerhofÂParnas pathway. In contrast, the direct and irreversible oxidation of D-glyceraldehyde 3-phosphate to 3-phospho-D-glycerate without production of ATP is catalysed either by non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase or by glyceraldehyde-3-phosphate ferredoxin oxidoreductase (EC 1.2.7.6). The non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase/glyceraldehyde-3-phosphate ferredoxin oxidoreductase substitution in the catabolic EmbdenÂMeyerhofÂParnas pathway avoids the production of the highly thermolabile compound 1,3-diphosphoglycerate and could minimize the pools of the thermolabile intermediates D-glyceraldehyde 3-phosphate and dihydroxyacetonphosphate by driving the carbon flow down the pathway and thus reducing the velocity of their heat destruction |
Thermoproteus tenax |
3-phospho-D-glycerate + NAD(P)H + 2 H+ |
- |
ir |
1.2.1.90 | D-glyceraldehyde 3-phosphate + NAD+ + H2O |
- |
Thermoproteus tenax |
3-phospho-D-glycerate + NADH + 2 H+ |
- |
ir |
1.2.1.90 | D-glyceraldehyde 3-phosphate + NAD+ + H2O |
- |
Nitrosomonas europaea |
3-phospho-D-glycerate + NADH + 2 H+ |
- |
ir |
1.2.1.90 | D-glyceraldehyde 3-phosphate + NAD+ + H2O |
part of the modified Emden-Meyerhof-Parnas pathway in Thermoproteus tenax |
Thermoproteus tenax |
3-phospho-D-glycerate + NADH + 2 H+ |
- |
ir |
1.2.1.90 | D-glyceraldehyde 3-phosphate + NAD+ + H2O |
the enzyme is part of the modified EmbdenÂMeyerhofÂParnas pathway, the main route for carbohydrate metabolism in Thermoproteus tenax |
Thermoproteus tenax |
3-phospho-D-glycerate + NADH + 2 H+ |
- |
ir |
1.2.1.90 | D-glyceraldehyde 3-phosphate + NAD+ + H2O |
the enzyme is able to utilize NAD+ and NADP+ as cofactor. Without activator Vmax of the NADP-dependent reaction is 40% compared to the NAD+-dependent reaction. In presence of activators (D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP) Vmax of the NADP+-dependent reaction increases by a factor of 3 |
Thermoproteus tenax |
3-phospho-D-glycerate + NADH + 2 H+ |
- |
ir |
1.2.1.90 | D-glyceraldehyde 3-phosphate + NADP+ + H2O |
- |
Nitrosomonas europaea |
3-phospho-D-glycerate + NADPH + 2 H+ |
- |
ir |
1.2.1.90 | D-glyceraldehyde 3-phosphate + NADP+ + H2O |
the enzyme is able to utilize NAD+ and NADP+ as cofactor. Without activator Vmax of the NADP-dependent reaction is 40% compared to the NAD+-dependent reaction. In presence of activators (D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP) Vmax of the NADP+-dependent reaction increases by a factor of 3 |
Thermoproteus tenax |
3-phospho-D-glycerate + NADPH + 2 H+ |
- |
ir |
1.2.1.90 | L-glyceraldehyde 3-phosphate + NAD+ + H2O |
- |
Nitrosomonas europaea |
3-phospho-L-glycerate + NADH + 2 H+ |
- |
ir |
1.2.1.90 | L-glyceraldehyde 3-phosphate + NADP+ + H2O |
- |
Nitrosomonas europaea |
3-phospho-L-glycerate + NADPH + 2 H+ |
- |
ir |